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• W2022682804 abstract "We have investigated the mechanism by which heat shock conditions lead to a reversible accumulation of trehalose in growing yeast. When cells of S. cerevisiae MI growing exponentially at 30°C were shifted to 45°C for 20 min, or to 39°C for 40 min, the concentration of trehalose increased by about 25‐fold; an effect reversed upon lowering the temperature to 30°C. This was compared to the more than 50‐fold rise in trehalose levels obtained upon transition from the exponential to the stationary growth phase. Whereas the latter was paralleled by a 12‐fold increase in the activity of trehalose‐6‐phosphate synthase, no significant change in the activities of trehalose‐synthesizing and ‐degrading enzymes was measured under heat shock conditions. Accordingly, cycloheximide did not prevent the heat‐induced accumulation of trehalose. However, the concentrations of the substrates for trehalose‐6‐phosphate synthase, i.e. glucose‐6‐phosphate and UDP‐glucose, were found to rise during heat shock by about 5–10‐fold. Since the elevated levels of both sugars are still well below the K m ‐values determined for trehalose‐6‐phosphate synthase in vitro, they are likely to contribute to the increase in trehalose under heat shock conditions. A similar increase in the steady‐state levels was obtained for other intermediates of the glycolytic pathway between glucose and triosephosphate, including ATP. This suggests that temperature‐dependent changes in the kinetic parameters of glycolytic enzymes vary in steady‐state levels of intermediates of sugar metabolism, including an increase of those that are required for trehalose synthesis. Trehalose, glucose‐6‐phosphate, UDP‐glucose, and ATP, were all found to increase during the 40 min heat treatment at 39°C. Since this also occurs in a mutant lacking the heat shock‐induced protein HSP104 (Δ hsp104 ), this protein cannot be involved in the accumulation of trehalose under these heat shock conditions. However, mutant Δ hsp104 , in contrast to the parental wild‐type, was sensitive towards a 20 min incubation at 50°C. Since this mutant also accumulated normal levels of trehalose, we conclude that HSP104 function, and not the accumulation of trehalose, protects S. cerevisiae from the damage caused by a 50°C treatment." @default.
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• W2022682804 date "1991-10-21" @default.
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• W2022682804 title "Metabolic regulation of the trehalose content of vegetative yeast" @default.
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• W2022682804 doi "https://doi.org/10.1016/0014-5793(91)81299-n" @default.
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